eF-site ID 2e8t-AB
PDB Code 2e8t
Chain A, B

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Title S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with magnesium, FsPP and IPP
Classification TRANSFERASE
Compound Geranylgeranyl pyrophosphate synthetase
Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (GGPPS_YEAST)
Sequence A:  NKMEAKIDELINNDPVWSSQNESLISKPYNHILLKRLNLI
VQINRVMNLPKDQLAIVSQIVELLHNSSLLIDDIEDNAPL
RRGQTTSHLIFGVPSTINTANYMYFRAMQLVSQLTTKEPL
YHNLITIFNEELINLHRGQGLDIYWRDFLPEIIPTQEMYL
NMVMNKTGGLFRLTLRLMEALSPSHGHSLVPFINLLGIIY
QIRDDYLNLKDFQGFAEDITEGKLSFPIVHALNFTKTKGQ
TEQHNEILRILLLRTSDKDIKLKLIQILEFDTNSLAYTKN
FINQLVNMIKNDNENKYLP
B:  KMEAKIDELINNDPVWSSQNESLISKPYNHILLKRLNLIV
QINRVMNLPKDQLAIVSQIVELLHNSSLLIDDIEDNAPLR
RGQTTSHLIFGVPSTINTANYMYFRAMQLVSQLTTKEPLY
HNLITIFNEELINLHRGQGLDIYWRDFLPEIIPTQEMYLN
MVMNKTGGLFRLTLRLMEALSPSHSLVPFINLLGIIYQIR
DDYLNLKDFQFAEDITEGKLSFPIVHALNFTKTKGQTEQH
NEILRILLLRTSDKDIKLKLIQILEFDTNSLAYTKNFINQ
LVNMIKNDNENKYLP
Description


Functional site

1) chain A
residue 80
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1301
source : AC1

2) chain A
residue 84
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1301
source : AC1

3) chain A
residue 80
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1302
source : AC2

4) chain A
residue 84
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1302
source : AC2

5) chain B
residue 80
type
sequence D
description BINDING SITE FOR RESIDUE MG B 1303
source : AC3

6) chain B
residue 84
type
sequence D
description BINDING SITE FOR RESIDUE MG B 1303
source : AC3

7) chain B
residue 80
type
sequence D
description BINDING SITE FOR RESIDUE MG B 1304
source : AC4

8) chain B
residue 84
type
sequence D
description BINDING SITE FOR RESIDUE MG B 1304
source : AC4

9) chain A
residue 44
type
sequence R
description BINDING SITE FOR RESIDUE IPE A 1001
source : AC5

10) chain A
residue 73
type
sequence H
description BINDING SITE FOR RESIDUE IPE A 1001
source : AC5

11) chain A
residue 90
type
sequence R
description BINDING SITE FOR RESIDUE IPE A 1001
source : AC5

12) chain A
residue 210
type
sequence Y
description BINDING SITE FOR RESIDUE IPE A 1001
source : AC5

13) chain A
residue 211
type
sequence Q
description BINDING SITE FOR RESIDUE IPE A 1001
source : AC5

14) chain B
residue 38
type
sequence K
description BINDING SITE FOR RESIDUE IPE B 1002
source : AC6

15) chain B
residue 44
type
sequence R
description BINDING SITE FOR RESIDUE IPE B 1002
source : AC6

16) chain B
residue 73
type
sequence H
description BINDING SITE FOR RESIDUE IPE B 1002
source : AC6

17) chain B
residue 77
type
sequence L
description BINDING SITE FOR RESIDUE IPE B 1002
source : AC6

18) chain B
residue 90
type
sequence R
description BINDING SITE FOR RESIDUE IPE B 1002
source : AC6

19) chain B
residue 210
type
sequence Y
description BINDING SITE FOR RESIDUE IPE B 1002
source : AC6

20) chain B
residue 211
type
sequence Q
description BINDING SITE FOR RESIDUE IPE B 1002
source : AC6

21) chain B
residue 214
type
sequence D
description BINDING SITE FOR RESIDUE IPE B 1002
source : AC6

22) chain A
residue 72
type
sequence L
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

23) chain A
residue 76
type
sequence S
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

24) chain A
residue 77
type
sequence L
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

25) chain A
residue 80
type
sequence D
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

26) chain A
residue 84
type
sequence D
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

27) chain A
residue 89
type
sequence R
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

28) chain A
residue 112
type
sequence Y
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

29) chain A
residue 140
type
sequence L
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

30) chain A
residue 143
type
sequence L
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

31) chain A
residue 144
type
sequence H
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

32) chain A
residue 147
type
sequence Q
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

33) chain A
residue 174
type
sequence K
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

34) chain A
residue 178
type
sequence L
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

35) chain A
residue 211
type
sequence Q
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

36) chain A
residue 214
type
sequence D
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

37) chain A
residue 238
type
sequence K
description BINDING SITE FOR RESIDUE FPS A 1201
source : AC7

38) chain B
residue 72
type
sequence L
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

39) chain B
residue 76
type
sequence S
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

40) chain B
residue 77
type
sequence L
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

41) chain B
residue 80
type
sequence D
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

42) chain B
residue 89
type
sequence R
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

43) chain B
residue 112
type
sequence Y
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

44) chain B
residue 140
type
sequence L
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

45) chain B
residue 143
type
sequence L
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

46) chain B
residue 144
type
sequence H
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

47) chain B
residue 147
type
sequence Q
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

48) chain B
residue 174
type
sequence K
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

49) chain B
residue 211
type
sequence Q
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

50) chain B
residue 214
type
sequence D
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

51) chain B
residue 238
type
sequence K
description BINDING SITE FOR RESIDUE FPS B 1202
source : AC8

52) chain A
residue 238
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

53) chain B
residue 44
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

54) chain B
residue 73
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

55) chain B
residue 89
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

56) chain B
residue 90
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

57) chain B
residue 174
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

58) chain B
residue 175
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

59) chain B
residue 211
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

60) chain B
residue 218
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

61) chain A
residue 44
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

62) chain B
residue 238
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

63) chain A
residue 73
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

64) chain A
residue 89
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

65) chain A
residue 90
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

66) chain A
residue 174
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

67) chain A
residue 175
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

68) chain A
residue 211
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

69) chain A
residue 218
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI1

70) chain A
residue 80
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI2

71) chain A
residue 84
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI2

72) chain B
residue 80
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI2

73) chain B
residue 84
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895
source Swiss-Prot : SWS_FT_FI2

74) chain A
residue 112
type SITE
sequence Y
description Important for determining product chain length
source Swiss-Prot : SWS_FT_FI4

75) chain B
residue 112
type SITE
sequence Y
description Important for determining product chain length
source Swiss-Prot : SWS_FT_FI4

76) chain A
residue 206-218
type prosite
sequence LGIIYQIRDDYLN
description POLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. LGiiYQIrDDYlN
source prosite : PS00444

77) chain A
residue 77-91
type prosite
sequence LLIDDIEDNAPLRRG
description POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LLiDDie..DnaplRRG
source prosite : PS00723


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